EC Number   |
Protein Variants |
Reference |
|---|
   1.3.7.5 | C210A |
retains 90% relative to wild type |
674669 |
| 1.3.7.5 | C86A |
retains 90% activity relative to wild type |
-, 674669 |
| 1.3.7.5 | D102N |
exhibits 11% of wild type activity |
685125 |
| 1.3.7.5 | D102N |
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D102N. Spectra reveal a biliverdin radical with a very narrow g tensor. This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated |
698489 |
| 1.3.7.5 | D102N |
retains 11% activity relative to wild type |
674669 |
| 1.3.7.5 | D105N |
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D105N. Spectra reveal a biliverdin radical with a very narrow g tensor with principal values 2.00359(5), 2.00341(5), and 2.00218(5). This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated |
698489 |
| 1.3.7.5 | D105N |
site-directed mutagenesis |
724288 |
| 1.3.7.5 | D116N |
retains 11% activity relative to wild type |
674669 |
| 1.3.7.5 | D217N |
retains 87% relative to wild type |
-, 674669 |
| 1.3.7.5 | E73Q |
exhibits 20% of wild type activity |
685125 |
